Professor T D W Claridge

Research

My role in the CRL is as the Director of NMR Spectroscopy for Organic Chemistry & Chemical Biology which means I am responsible for managing the core NMR facilities, services and support staff. I am also professor of magnetic resonance and my research interests revolve around the application of solution-state NMR techniques to address questions of structure, function and dynamics of "small" molecules in organic chemistry and chemical biology. Many of the projects in which I become involved arise through collaborations with groups across the department and the university more widely.

Protein-ligand binding studies by NMR Spectroscopy

The interaction of small molecules with protein targets is an area in which NMR spectroscopy can play a key role, providing information on the behavior of the small molecule and on structural changes in the protein itself. A wide range of techniques are available to probe such interactions (such as saturation transfer difference and WaterLOGSY) and we are interested in further developing and applying such methods to a variety biological systems. We also employ protein-observe methods when isotopically labelled macromolecules are available. We apply these methods to 2-oxoglutarate dependent Fe(II) enzymes, in collaboration with Prof. Chris Schofield.

NMR methods for studying small molecules

Despite their relatively small size, many molecules encountered in the laboratory of synthetic and medicinal chemists have structures that can prove surprisingly difficult to define reliably, especially in relation to stereochemistry. We are interested in exploring the application of novel methods and developing these further to help better elucidate small molecule structures. Methods that are currently of interest are those based on pure shift methodology (broadband proton decoupled proton spectroscopy), methods for fluorinated molecules, and the use of residual dipolar couplings (RDCs) as alternatives to traditional scalar couplings and NOEs.